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1 INTRODUCTION The binding of metal ions by proteins and pep- tides is of fundamental interest due to the impor- tance of metal ions in biological systems. Metals may be part of the active sites of enzymes, stabilize the macromolecular structure of proteins and affect enzymes or membranes to control cell metabolism[1]. Therefore, for many years there has been a great in- terest in the study of complexes able to mimic these active sites of metalloproteins. In this case, metal complexes of… 相似文献
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Using Cu(Ⅱ) as the template, a complex {[Cu2L2(H2O)2] 4H2O}n (L = N-acetoxyl-
picolinamide) has been successfully synthesized and characterized by single-crystal X-ray diffrac
tion. The crystal is of monoclinic, space group C2/c, with a = 24.144(5), b = 7.1622(14), c =
17.283(4) (A), C16H24Cu2N4O12, Mr = 591.47, β = 131.73(3)°, V = 2230.3(8) (A)3, Z = 4, Dc= 1.761
g/cm3, F(000) = 1208,μ = 1.978 mm-1, R = 0.0400 and wR = 0.1099. The copper (Ⅱ) ion is five
coordinated with a distorted square pyramidal geometry. The complex can be viewed as a one
dimensional chain structure by carboxylic bridges among copper atoms. In the complex there exist
hydrogen bonding interactions to stabilize the structure. 相似文献
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